Work has been carried out on a number of structural problems related to proteins derived from the HIV-1 virus. We showed by NMR that autoprocessing of the HIV-1 precursor is tightly coupled to protein folding. Only after cleavage at the mature N-terminus is a stable structure formed which exhibits activity. In addition, novel methodological approaches and media for partially aligning macromolecules to measure residual dipolar couplings were developed and applied to a variety of systems. In particular, the potent HIV-inactivating molecule cyanovirin-N was studied under extreme conditions.